KR20000070256A - 라미닌의 니도겐-결합 도메인에 결합하는 항체, 이의 제조방법및 용도 - Google Patents
라미닌의 니도겐-결합 도메인에 결합하는 항체, 이의 제조방법및 용도 Download PDFInfo
- Publication number
- KR20000070256A KR20000070256A KR1019997006484A KR19997006484A KR20000070256A KR 20000070256 A KR20000070256 A KR 20000070256A KR 1019997006484 A KR1019997006484 A KR 1019997006484A KR 19997006484 A KR19997006484 A KR 19997006484A KR 20000070256 A KR20000070256 A KR 20000070256A
- Authority
- KR
- South Korea
- Prior art keywords
- laminin
- antibody
- nidogen
- binding
- iii
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Withdrawn
Links
- 238000009739 binding Methods 0.000 title claims abstract description 113
- 230000027455 binding Effects 0.000 title claims abstract description 111
- 108010008217 nidogen Proteins 0.000 title claims abstract description 103
- 238000004519 manufacturing process Methods 0.000 title claims description 10
- 108010085895 Laminin Proteins 0.000 claims abstract description 102
- 102000007547 Laminin Human genes 0.000 claims abstract description 102
- 238000000034 method Methods 0.000 claims abstract description 25
- 230000003993 interaction Effects 0.000 claims abstract description 16
- 239000000463 material Substances 0.000 claims abstract description 16
- 239000003814 drug Substances 0.000 claims abstract description 14
- 239000000032 diagnostic agent Substances 0.000 claims abstract description 10
- 229940039227 diagnostic agent Drugs 0.000 claims abstract description 10
- 230000002401 inhibitory effect Effects 0.000 claims abstract description 6
- 108010018737 laminin P1 Proteins 0.000 claims description 64
- 108010090909 laminin gamma 1 Proteins 0.000 claims description 63
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 53
- 230000003053 immunization Effects 0.000 claims description 32
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 31
- 239000000427 antigen Substances 0.000 claims description 25
- 102000036639 antigens Human genes 0.000 claims description 25
- 108091007433 antigens Proteins 0.000 claims description 25
- 238000002649 immunization Methods 0.000 claims description 23
- 210000004408 hybridoma Anatomy 0.000 claims description 21
- 210000004027 cell Anatomy 0.000 claims description 17
- 238000001042 affinity chromatography Methods 0.000 claims description 13
- 239000011159 matrix material Substances 0.000 claims description 13
- 239000012528 membrane Substances 0.000 claims description 11
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 10
- 238000012360 testing method Methods 0.000 claims description 10
- 241000251539 Vertebrata <Metazoa> Species 0.000 claims description 9
- 239000000126 substance Substances 0.000 claims description 9
- 201000010099 disease Diseases 0.000 claims description 8
- 230000015572 biosynthetic process Effects 0.000 claims description 7
- 239000002671 adjuvant Substances 0.000 claims description 6
- 238000011161 development Methods 0.000 claims description 5
- 230000000144 pharmacologic effect Effects 0.000 claims description 5
- 238000003786 synthesis reaction Methods 0.000 claims description 5
- 230000001419 dependent effect Effects 0.000 claims description 4
- 230000033115 angiogenesis Effects 0.000 claims description 3
- 230000002860 competitive effect Effects 0.000 claims description 3
- 208000002249 Diabetes Complications Diseases 0.000 claims description 2
- 206010012689 Diabetic retinopathy Diseases 0.000 claims description 2
- 206010016654 Fibrosis Diseases 0.000 claims description 2
- 206010028980 Neoplasm Diseases 0.000 claims description 2
- 201000004681 Psoriasis Diseases 0.000 claims description 2
- 206010047115 Vasculitis Diseases 0.000 claims description 2
- 230000001476 alcoholic effect Effects 0.000 claims description 2
- 239000012472 biological sample Substances 0.000 claims description 2
- 210000001124 body fluid Anatomy 0.000 claims description 2
- 239000010839 body fluid Substances 0.000 claims description 2
- 201000011510 cancer Diseases 0.000 claims description 2
- 208000019425 cirrhosis of liver Diseases 0.000 claims description 2
- 230000004761 fibrosis Effects 0.000 claims description 2
- 230000002757 inflammatory effect Effects 0.000 claims description 2
- 201000008482 osteoarthritis Diseases 0.000 claims description 2
- 230000003389 potentiating effect Effects 0.000 claims description 2
- 208000005069 pulmonary fibrosis Diseases 0.000 claims description 2
- 206010039073 rheumatoid arthritis Diseases 0.000 claims description 2
- 230000008719 thickening Effects 0.000 claims description 2
- 125000003275 alpha amino acid group Chemical group 0.000 claims 2
- 201000001320 Atherosclerosis Diseases 0.000 claims 1
- 208000007342 Diabetic Nephropathies Diseases 0.000 claims 1
- 206010012655 Diabetic complications Diseases 0.000 claims 1
- 208000033679 diabetic kidney disease Diseases 0.000 claims 1
- 238000011156 evaluation Methods 0.000 claims 1
- 230000036961 partial effect Effects 0.000 claims 1
- 238000002360 preparation method Methods 0.000 abstract description 13
- 102000001708 Protein Isoforms Human genes 0.000 abstract description 2
- 108010029485 Protein Isoforms Proteins 0.000 abstract description 2
- 239000000243 solution Substances 0.000 description 22
- 108010058846 Ovalbumin Proteins 0.000 description 17
- 239000000562 conjugate Substances 0.000 description 17
- 230000005764 inhibitory process Effects 0.000 description 16
- 239000002953 phosphate buffered saline Substances 0.000 description 15
- 239000011734 sodium Substances 0.000 description 14
- 150000001413 amino acids Chemical class 0.000 description 13
- 238000003556 assay Methods 0.000 description 13
- 241001465754 Metazoa Species 0.000 description 12
- 210000002966 serum Anatomy 0.000 description 12
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 11
- 241000283973 Oryctolagus cuniculus Species 0.000 description 11
- 239000003112 inhibitor Substances 0.000 description 11
- 241000699670 Mus sp. Species 0.000 description 10
- 239000000203 mixture Substances 0.000 description 10
- 238000006243 chemical reaction Methods 0.000 description 9
- 230000028993 immune response Effects 0.000 description 9
- 210000004379 membrane Anatomy 0.000 description 9
- 229920001213 Polysorbate 20 Polymers 0.000 description 8
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 8
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 8
- 239000000872 buffer Substances 0.000 description 7
- 239000012228 culture supernatant Substances 0.000 description 7
- 238000009472 formulation Methods 0.000 description 7
- 238000011534 incubation Methods 0.000 description 7
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 6
- 241000700159 Rattus Species 0.000 description 6
- 239000012634 fragment Substances 0.000 description 6
- 230000003169 placental effect Effects 0.000 description 6
- 241000699666 Mus <mouse, genus> Species 0.000 description 5
- 238000003018 immunoassay Methods 0.000 description 5
- 108090000623 proteins and genes Proteins 0.000 description 5
- 238000001262 western blot Methods 0.000 description 5
- 208000009331 Experimental Sarcoma Diseases 0.000 description 4
- 229910019142 PO4 Inorganic materials 0.000 description 4
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 4
- 238000004458 analytical method Methods 0.000 description 4
- 238000004113 cell culture Methods 0.000 description 4
- 238000004587 chromatography analysis Methods 0.000 description 4
- 238000010367 cloning Methods 0.000 description 4
- 230000018109 developmental process Effects 0.000 description 4
- 230000004927 fusion Effects 0.000 description 4
- 239000000499 gel Substances 0.000 description 4
- 238000005259 measurement Methods 0.000 description 4
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 4
- 239000010452 phosphate Substances 0.000 description 4
- 102000004169 proteins and genes Human genes 0.000 description 4
- 238000000746 purification Methods 0.000 description 4
- 239000011347 resin Substances 0.000 description 4
- 229920005989 resin Polymers 0.000 description 4
- 238000012216 screening Methods 0.000 description 4
- 241000283707 Capra Species 0.000 description 3
- 241000700198 Cavia Species 0.000 description 3
- 102000004190 Enzymes Human genes 0.000 description 3
- 108090000790 Enzymes Proteins 0.000 description 3
- 241000287828 Gallus gallus Species 0.000 description 3
- 239000004471 Glycine Substances 0.000 description 3
- 241001494479 Pecora Species 0.000 description 3
- 239000007864 aqueous solution Substances 0.000 description 3
- 235000013330 chicken meat Nutrition 0.000 description 3
- 230000000295 complement effect Effects 0.000 description 3
- 150000001875 compounds Chemical class 0.000 description 3
- 238000001514 detection method Methods 0.000 description 3
- 230000002255 enzymatic effect Effects 0.000 description 3
- 238000001502 gel electrophoresis Methods 0.000 description 3
- 238000012986 modification Methods 0.000 description 3
- 230000004048 modification Effects 0.000 description 3
- 239000002808 molecular sieve Substances 0.000 description 3
- 238000000159 protein binding assay Methods 0.000 description 3
- URGAHOPLAPQHLN-UHFFFAOYSA-N sodium aluminosilicate Chemical compound [Na+].[Al+3].[O-][Si]([O-])=O.[O-][Si]([O-])=O URGAHOPLAPQHLN-UHFFFAOYSA-N 0.000 description 3
- 241000894007 species Species 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- ZCYVEMRRCGMTRW-UHFFFAOYSA-N 7553-56-2 Chemical compound [I] ZCYVEMRRCGMTRW-UHFFFAOYSA-N 0.000 description 2
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 2
- 206010003445 Ascites Diseases 0.000 description 2
- CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 description 2
- 102000014914 Carrier Proteins Human genes 0.000 description 2
- 108010078791 Carrier Proteins Proteins 0.000 description 2
- 241000255581 Drosophila <fruit fly, genus> Species 0.000 description 2
- 238000002965 ELISA Methods 0.000 description 2
- 102000003886 Glycoproteins Human genes 0.000 description 2
- 108090000288 Glycoproteins Proteins 0.000 description 2
- 241000282412 Homo Species 0.000 description 2
- 206010035226 Plasma cell myeloma Diseases 0.000 description 2
- 239000002202 Polyethylene glycol Substances 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 2
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 2
- 238000001261 affinity purification Methods 0.000 description 2
- 239000000556 agonist Substances 0.000 description 2
- 150000001718 carbodiimides Chemical class 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 230000000052 comparative effect Effects 0.000 description 2
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 210000002969 egg yolk Anatomy 0.000 description 2
- 239000000839 emulsion Substances 0.000 description 2
- 238000010353 genetic engineering Methods 0.000 description 2
- PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 description 2
- 239000010931 gold Substances 0.000 description 2
- 229910052737 gold Inorganic materials 0.000 description 2
- XMBWDFGMSWQBCA-UHFFFAOYSA-N hydrogen iodide Chemical compound I XMBWDFGMSWQBCA-UHFFFAOYSA-N 0.000 description 2
- FDGQSTZJBFJUBT-UHFFFAOYSA-N hypoxanthine Chemical compound O=C1NC=NC2=C1NC=N2 FDGQSTZJBFJUBT-UHFFFAOYSA-N 0.000 description 2
- 210000002865 immune cell Anatomy 0.000 description 2
- 210000000987 immune system Anatomy 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- 238000002347 injection Methods 0.000 description 2
- 239000007924 injection Substances 0.000 description 2
- 229910052740 iodine Inorganic materials 0.000 description 2
- 239000011630 iodine Substances 0.000 description 2
- 239000003446 ligand Substances 0.000 description 2
- 244000005700 microbiome Species 0.000 description 2
- 230000000877 morphologic effect Effects 0.000 description 2
- 201000000050 myeloid neoplasm Diseases 0.000 description 2
- 150000007523 nucleic acids Chemical group 0.000 description 2
- 239000000863 peptide conjugate Substances 0.000 description 2
- 230000003285 pharmacodynamic effect Effects 0.000 description 2
- 239000008363 phosphate buffer Substances 0.000 description 2
- 210000002826 placenta Anatomy 0.000 description 2
- 229920002401 polyacrylamide Polymers 0.000 description 2
- 229920001223 polyethylene glycol Polymers 0.000 description 2
- 210000001236 prokaryotic cell Anatomy 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- 239000000523 sample Substances 0.000 description 2
- 238000012882 sequential analysis Methods 0.000 description 2
- 210000004989 spleen cell Anatomy 0.000 description 2
- 238000010561 standard procedure Methods 0.000 description 2
- KZNICNPSHKQLFF-UHFFFAOYSA-N succinimide Chemical compound O=C1CCC(=O)N1 KZNICNPSHKQLFF-UHFFFAOYSA-N 0.000 description 2
- 239000013589 supplement Substances 0.000 description 2
- 230000001629 suppression Effects 0.000 description 2
- 229940124597 therapeutic agent Drugs 0.000 description 2
- 238000012546 transfer Methods 0.000 description 2
- 230000007704 transition Effects 0.000 description 2
- AQRLNPVMDITEJU-UHFFFAOYSA-N triethylsilane Chemical compound CC[SiH](CC)CC AQRLNPVMDITEJU-UHFFFAOYSA-N 0.000 description 2
- IEJPPSMHUUQABK-UHFFFAOYSA-N 2,4-diphenyl-4h-1,3-oxazol-5-one Chemical compound O=C1OC(C=2C=CC=CC=2)=NC1C1=CC=CC=C1 IEJPPSMHUUQABK-UHFFFAOYSA-N 0.000 description 1
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 1
- TVZGACDUOSZQKY-LBPRGKRZSA-N 4-aminofolic acid Chemical compound C1=NC2=NC(N)=NC(N)=C2N=C1CNC1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 TVZGACDUOSZQKY-LBPRGKRZSA-N 0.000 description 1
- 125000003143 4-hydroxybenzyl group Chemical group [H]C([*])([H])C1=C([H])C([H])=C(O[H])C([H])=C1[H] 0.000 description 1
- ZZOKVYOCRSMTSS-UHFFFAOYSA-M 9h-fluoren-9-ylmethoxymethanimidate Chemical compound C1=CC=C2C(COC(=O)[NH-])C3=CC=CC=C3C2=C1 ZZOKVYOCRSMTSS-UHFFFAOYSA-M 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 102000009027 Albumins Human genes 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- ATRRKUHOCOJYRX-UHFFFAOYSA-N Ammonium bicarbonate Chemical compound [NH4+].OC([O-])=O ATRRKUHOCOJYRX-UHFFFAOYSA-N 0.000 description 1
- 229910000013 Ammonium bicarbonate Inorganic materials 0.000 description 1
- 206010003210 Arteriosclerosis Diseases 0.000 description 1
- 238000000035 BCA protein assay Methods 0.000 description 1
- DWRXFEITVBNRMK-UHFFFAOYSA-N Beta-D-1-Arabinofuranosylthymine Natural products O=C1NC(=O)C(C)=CN1C1C(O)C(O)C(CO)O1 DWRXFEITVBNRMK-UHFFFAOYSA-N 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- BVKZGUZCCUSVTD-UHFFFAOYSA-L Carbonate Chemical compound [O-]C([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-L 0.000 description 1
- 208000005623 Carcinogenesis Diseases 0.000 description 1
- 208000032862 Clinical Deterioration Diseases 0.000 description 1
- 102000004266 Collagen Type IV Human genes 0.000 description 1
- 108010042086 Collagen Type IV Proteins 0.000 description 1
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 1
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 1
- 108010000912 Egg Proteins Proteins 0.000 description 1
- 102000002322 Egg Proteins Human genes 0.000 description 1
- 102400001368 Epidermal growth factor Human genes 0.000 description 1
- 101800003838 Epidermal growth factor Proteins 0.000 description 1
- 108050001049 Extracellular proteins Proteins 0.000 description 1
- 239000007995 HEPES buffer Substances 0.000 description 1
- UGQMRVRMYYASKQ-UHFFFAOYSA-N Hypoxanthine nucleoside Natural products OC1C(O)C(CO)OC1N1C(NC=NC2=O)=C2N=C1 UGQMRVRMYYASKQ-UHFFFAOYSA-N 0.000 description 1
- 108060003951 Immunoglobulin Proteins 0.000 description 1
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 1
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 1
- 239000007993 MOPS buffer Substances 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 108091028043 Nucleic acid sequence Proteins 0.000 description 1
- 102000015636 Oligopeptides Human genes 0.000 description 1
- 108010038807 Oligopeptides Proteins 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 239000004372 Polyvinyl alcohol Substances 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 229920005654 Sephadex Polymers 0.000 description 1
- 239000012507 Sephadex™ Substances 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- UIIMBOGNXHQVGW-DEQYMQKBSA-M Sodium bicarbonate-14C Chemical compound [Na+].O[14C]([O-])=O UIIMBOGNXHQVGW-DEQYMQKBSA-M 0.000 description 1
- 101710120037 Toxin CcdB Proteins 0.000 description 1
- 101150117115 V gene Proteins 0.000 description 1
- 239000013543 active substance Substances 0.000 description 1
- 230000002730 additional effect Effects 0.000 description 1
- 229960003896 aminopterin Drugs 0.000 description 1
- 235000012538 ammonium bicarbonate Nutrition 0.000 description 1
- 239000001099 ammonium carbonate Substances 0.000 description 1
- 239000005557 antagonist Substances 0.000 description 1
- 208000011775 arteriosclerosis disease Diseases 0.000 description 1
- 229960005070 ascorbic acid Drugs 0.000 description 1
- 235000010323 ascorbic acid Nutrition 0.000 description 1
- 239000011668 ascorbic acid Substances 0.000 description 1
- 150000001540 azides Chemical class 0.000 description 1
- 210000002469 basement membrane Anatomy 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- IQFYYKKMVGJFEH-UHFFFAOYSA-N beta-L-thymidine Natural products O=C1NC(=O)C(C)=CN1C1OC(CO)C(O)C1 IQFYYKKMVGJFEH-UHFFFAOYSA-N 0.000 description 1
- 230000007321 biological mechanism Effects 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 230000036952 cancer formation Effects 0.000 description 1
- 231100000504 carcinogenesis Toxicity 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 210000001175 cerebrospinal fluid Anatomy 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- VDQQXEISLMTGAB-UHFFFAOYSA-N chloramine T Chemical compound [Na+].CC1=CC=C(S(=O)(=O)[N-]Cl)C=C1 VDQQXEISLMTGAB-UHFFFAOYSA-N 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 239000012141 concentrate Substances 0.000 description 1
- 238000009833 condensation Methods 0.000 description 1
- 230000005494 condensation Effects 0.000 description 1
- 108091036078 conserved sequence Proteins 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 230000037029 cross reaction Effects 0.000 description 1
- 230000009260 cross reactivity Effects 0.000 description 1
- 239000013078 crystal Substances 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- 238000010494 dissociation reaction Methods 0.000 description 1
- 230000005593 dissociations Effects 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- 150000002019 disulfides Chemical class 0.000 description 1
- WBZKQQHYRPRKNJ-UHFFFAOYSA-L disulfite Chemical compound [O-]S(=O)S([O-])(=O)=O WBZKQQHYRPRKNJ-UHFFFAOYSA-L 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 235000013345 egg yolk Nutrition 0.000 description 1
- 230000013020 embryo development Effects 0.000 description 1
- 210000002257 embryonic structure Anatomy 0.000 description 1
- 229940116977 epidermal growth factor Drugs 0.000 description 1
- 210000002615 epidermis Anatomy 0.000 description 1
- 239000003797 essential amino acid Substances 0.000 description 1
- 235000020776 essential amino acid Nutrition 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 238000013100 final test Methods 0.000 description 1
- 239000003102 growth factor Substances 0.000 description 1
- 108060003552 hemocyanin Proteins 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 230000000984 immunochemical effect Effects 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 230000005847 immunogenicity Effects 0.000 description 1
- 102000018358 immunoglobulin Human genes 0.000 description 1
- 230000016784 immunoglobulin production Effects 0.000 description 1
- 229940072221 immunoglobulins Drugs 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 210000001165 lymph node Anatomy 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- SJUGPXBWZCQTKM-UHFFFAOYSA-N n-chloro-4-methylbenzenesulfonamide;sodium Chemical compound [Na].CC1=CC=C(S(=O)(=O)NCl)C=C1 SJUGPXBWZCQTKM-UHFFFAOYSA-N 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 230000005305 organ development Effects 0.000 description 1
- 229940092253 ovalbumin Drugs 0.000 description 1
- 230000005298 paramagnetic effect Effects 0.000 description 1
- 238000010647 peptide synthesis reaction Methods 0.000 description 1
- 239000012071 phase Substances 0.000 description 1
- 230000035790 physiological processes and functions Effects 0.000 description 1
- 210000002381 plasma Anatomy 0.000 description 1
- 229920003023 plastic Polymers 0.000 description 1
- 239000004033 plastic Substances 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 229920002451 polyvinyl alcohol Polymers 0.000 description 1
- 238000011533 pre-incubation Methods 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 238000000163 radioactive labelling Methods 0.000 description 1
- 238000003127 radioimmunoassay Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000002829 reductive effect Effects 0.000 description 1
- 238000004007 reversed phase HPLC Methods 0.000 description 1
- 238000002390 rotary evaporation Methods 0.000 description 1
- 210000003296 saliva Anatomy 0.000 description 1
- 229920006395 saturated elastomer Polymers 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 230000015607 signal release Effects 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- RPACBEVZENYWOL-XFULWGLBSA-M sodium;(2r)-2-[6-(4-chlorophenoxy)hexyl]oxirane-2-carboxylate Chemical compound [Na+].C=1C=C(Cl)C=CC=1OCCCCCC[C@]1(C(=O)[O-])CO1 RPACBEVZENYWOL-XFULWGLBSA-M 0.000 description 1
- 238000010532 solid phase synthesis reaction Methods 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 230000003393 splenic effect Effects 0.000 description 1
- 230000006641 stabilisation Effects 0.000 description 1
- 238000011105 stabilization Methods 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 229960002317 succinimide Drugs 0.000 description 1
- 238000002198 surface plasmon resonance spectroscopy Methods 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 239000010409 thin film Substances 0.000 description 1
- 229940104230 thymidine Drugs 0.000 description 1
- 210000002700 urine Anatomy 0.000 description 1
- VBEQCZHXXJYVRD-GACYYNSASA-N uroanthelone Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CS)C(=O)N[C@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O)C(C)C)[C@@H](C)O)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CCSC)NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)CNC(=O)CNC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CS)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CS)NC(=O)CNC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC(N)=O)C(C)C)[C@@H](C)CC)C1=CC=C(O)C=C1 VBEQCZHXXJYVRD-GACYYNSASA-N 0.000 description 1
- 230000002792 vascular Effects 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 238000005303 weighing Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P11/00—Drugs for disorders of the respiratory system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P13/00—Drugs for disorders of the urinary system
- A61P13/12—Drugs for disorders of the urinary system of the kidneys
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
- A61P17/06—Antipsoriatics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A61P19/02—Drugs for skeletal disorders for joint disorders, e.g. arthritis, arthrosis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P27/00—Drugs for disorders of the senses
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P29/00—Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
- A61P3/08—Drugs for disorders of the metabolism for glucose homeostasis
- A61P3/10—Drugs for disorders of the metabolism for glucose homeostasis for hyperglycaemia, e.g. antidiabetics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
- A61P9/10—Drugs for disorders of the cardiovascular system for treating ischaemic or atherosclerotic diseases, e.g. antianginal drugs, coronary vasodilators, drugs for myocardial infarction, retinopathy, cerebrovascula insufficiency, renal arteriosclerosis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Medicinal Chemistry (AREA)
- Veterinary Medicine (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Pharmacology & Pharmacy (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Immunology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Diabetes (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Urology & Nephrology (AREA)
- Heart & Thoracic Surgery (AREA)
- Cardiology (AREA)
- Rheumatology (AREA)
- Emergency Medicine (AREA)
- Orthopedic Medicine & Surgery (AREA)
- Physical Education & Sports Medicine (AREA)
- Pulmonology (AREA)
- Endocrinology (AREA)
- Hematology (AREA)
- Obesity (AREA)
- Pain & Pain Management (AREA)
- Dermatology (AREA)
- Vascular Medicine (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Investigating Or Analysing Biological Materials (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DE19701607.3 | 1997-01-17 | ||
| DE19701607A DE19701607A1 (de) | 1997-01-17 | 1997-01-17 | Anitkörper, die an die Nidogen-Bindungsdomäne des Laminins binden, deren Herstellung und Verwendung |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| KR20000070256A true KR20000070256A (ko) | 2000-11-25 |
Family
ID=7817701
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| KR1019997006484A Withdrawn KR20000070256A (ko) | 1997-01-17 | 1997-12-22 | 라미닌의 니도겐-결합 도메인에 결합하는 항체, 이의 제조방법및 용도 |
Country Status (18)
| Country | Link |
|---|---|
| US (1) | US20010007020A1 (cs) |
| EP (1) | EP0954535A1 (cs) |
| JP (1) | JP2001509020A (cs) |
| KR (1) | KR20000070256A (cs) |
| CN (1) | CN1244873A (cs) |
| AR (1) | AR011074A1 (cs) |
| AU (1) | AU5985398A (cs) |
| BR (1) | BR9714207A (cs) |
| CA (1) | CA2278477A1 (cs) |
| CZ (1) | CZ253899A3 (cs) |
| DE (1) | DE19701607A1 (cs) |
| HU (1) | HUP0001808A3 (cs) |
| ID (1) | ID21895A (cs) |
| IL (1) | IL130808A0 (cs) |
| PL (1) | PL334956A1 (cs) |
| TR (1) | TR199901648T2 (cs) |
| WO (1) | WO1998031709A1 (cs) |
| ZA (1) | ZA98367B (cs) |
Families Citing this family (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20030087318A1 (en) * | 1994-04-18 | 2003-05-08 | Lallone Roger L. | Antibodies against an extracellular matrix complex and their use in the detection of cancer |
| EP1070727A1 (en) | 1999-03-01 | 2001-01-24 | Aventis Pharma Deutschland GmbH | Low molecular weight peptide derivatives as inhibitors of the laminin/nidogen interaction |
| CA2389751A1 (en) * | 1999-11-01 | 2001-05-10 | Curagen Corporation | Differentially expressed genes involved in angiogenesis, the polypeptides encoded thereby, and methods of using the same |
| WO2001061349A1 (en) * | 2000-02-18 | 2001-08-23 | The University Of Tennessee Research Corporation | Detection of microbial deposition and immune response at the basement membrane |
| ATE331785T1 (de) * | 2000-03-29 | 2006-07-15 | Beth Israel Hospital | Anti-angiogenic properties of matin and of fragments or variants thereof |
| US20030119739A1 (en) * | 2000-03-29 | 2003-06-26 | Beth Israel Deaconess Medical Center | Anti-angiogenic and anti-tumor properties of Vascostatin and other nidogen domains |
| WO2004093892A2 (en) | 2003-04-16 | 2004-11-04 | Genentech, Inc. | Stanniocalcin-1, variant or antagonists thereof for selective modulation of vascularization |
| US20140045196A1 (en) * | 2012-08-13 | 2014-02-13 | University Of Tokyo | Methods of prognosis and diagnosis of cancer |
| CN110860766A (zh) * | 2019-10-22 | 2020-03-06 | 广东开放大学（广东理工职业学院） | 铝合金薄板的调制脉冲电流焊接方法、系统及存储介质 |
Family Cites Families (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5211657A (en) * | 1988-11-07 | 1993-05-18 | The United States Government As Represented By The Secretary Of The Department Of Health And Human Services | Laminin a chain deduced amino acid sequence, expression vectors and active synthetic peptides |
| ES2459290T3 (es) * | 1994-08-11 | 2014-05-08 | Sanofi-Aventis Deutschland Gmbh | Anticuerpos monoclonales para la determinación inmunológica selectiva de formas de lamininas de alto peso molecular en líquidos corporales |
| US5493008A (en) * | 1994-08-15 | 1996-02-20 | The University Of Virginia Patent Foundation | Two non-contiguous regions contribute to nidogen binding to a single EGF-like motif of the laminin γ1 chain |
-
1997
- 1997-01-17 DE DE19701607A patent/DE19701607A1/de not_active Withdrawn
- 1997-12-22 TR TR1999/01648T patent/TR199901648T2/xx unknown
- 1997-12-22 KR KR1019997006484A patent/KR20000070256A/ko not_active Withdrawn
- 1997-12-22 BR BR9714207-7A patent/BR9714207A/pt not_active IP Right Cessation
- 1997-12-22 ID IDW990701A patent/ID21895A/id unknown
- 1997-12-22 JP JP53230298A patent/JP2001509020A/ja active Pending
- 1997-12-22 US US09/341,643 patent/US20010007020A1/en not_active Abandoned
- 1997-12-22 AU AU59853/98A patent/AU5985398A/en not_active Abandoned
- 1997-12-22 PL PL97334956A patent/PL334956A1/xx unknown
- 1997-12-22 CN CN97181412A patent/CN1244873A/zh active Pending
- 1997-12-22 CA CA002278477A patent/CA2278477A1/en not_active Abandoned
- 1997-12-22 EP EP97954750A patent/EP0954535A1/de not_active Withdrawn
- 1997-12-22 CZ CZ992538A patent/CZ253899A3/cs unknown
- 1997-12-22 WO PCT/EP1997/007241 patent/WO1998031709A1/de not_active Ceased
- 1997-12-22 IL IL13080897A patent/IL130808A0/xx unknown
- 1997-12-22 HU HU0001808A patent/HUP0001808A3/hu unknown
-
1998
- 1998-01-15 AR ARP980100177A patent/AR011074A1/es unknown
- 1998-01-16 ZA ZA98367A patent/ZA98367B/xx unknown
Also Published As
| Publication number | Publication date |
|---|---|
| CN1244873A (zh) | 2000-02-16 |
| BR9714207A (pt) | 2000-03-28 |
| ZA98367B (en) | 1998-07-17 |
| CA2278477A1 (en) | 1998-07-23 |
| IL130808A0 (en) | 2001-01-28 |
| HUP0001808A2 (hu) | 2000-09-28 |
| US20010007020A1 (en) | 2001-07-05 |
| TR199901648T2 (xx) | 1999-10-21 |
| WO1998031709A1 (de) | 1998-07-23 |
| HUP0001808A3 (en) | 2001-09-28 |
| PL334956A1 (en) | 2000-03-27 |
| JP2001509020A (ja) | 2001-07-10 |
| AR011074A1 (es) | 2000-08-02 |
| AU5985398A (en) | 1998-08-07 |
| EP0954535A1 (de) | 1999-11-10 |
| DE19701607A1 (de) | 1998-07-23 |
| ID21895A (id) | 1999-08-05 |
| CZ253899A3 (cs) | 1999-10-13 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP7418508B2 (ja) | 抗プロ／潜在型ミオスタチン抗体およびその使用 | |
| US8673301B2 (en) | YKL-40 monoclonal antibody | |
| US8206706B2 (en) | Method for enhancing or inhibiting insulin-like growth factor-I | |
| WO2004031238A2 (en) | Antibodies and cyclic peptides which bind cea (carcinoembryonic antigen) and their use as cancer therapeutics | |
| JPH09124697A (ja) | ペプチド及びモノクローナル抗体 | |
| CN109988240A (zh) | 抗gpc-3抗体及其用途 | |
| KR101154550B1 (ko) | 폰 빌레브란트 인자 특이적 절단 효소에 대한 항체 및그것을 이용한 분석계 | |
| CA2635849A1 (en) | An antibody against periostin, and a pharmaceutical composition comprising it for preventing or treating a disease in which periostin is involved | |
| US9868787B2 (en) | Monoclonal antibodies for enhancing or inhibiting insulin-like growth factor-I | |
| KR20000070256A (ko) | 라미닌의 니도겐-결합 도메인에 결합하는 항체, 이의 제조방법및 용도 | |
| KR20140043795A (ko) | 가용성 인테그린 α4 변이체 | |
| US5811268A (en) | Monoclonal antibodies for selective immunological determination of high molecular weight, intact laminin forms in body fluids | |
| WO2017211313A1 (zh) | 长效pcsk9特异性的结合蛋白及其应用 | |
| Johnson et al. | Identification of an antigenic epitope and receptor binding domain of human C5a. | |
| KR20070042994A (ko) | 항시노비올린 항체 | |
| US20060024314A1 (en) | Antibodies and cyclic peptides which bind CEA (carcinoembryonic antigens) and their use as cancer therapeutics | |
| JPH06508743A (ja) | ヒトｔｎｆ結合タンパク質１（ｔｎｆ−ｂｐ １）に対するモノクローナル抗体 | |
| MXPA99006647A (en) | Antibodies that bind to the nidogen-binding domain of laminin, their production and use | |
| HK1024250A (en) | Antibodies that bind to the nidogen-binding domain of laminin, their production and use | |
| JPH05168494A (ja) | ハイブリッド・モノクローナル抗体および抗体含有薬剤 | |
| JP2004242671A (ja) | 抗体およびその用途 | |
| HK1084127B (en) | Recombinant anti-osteopontin antibody and use thereof |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PA0105 | International application |
Patent event date: 19990716 Patent event code: PA01051R01D Comment text: International Patent Application |
|
| PG1501 | Laying open of application | ||
| PC1203 | Withdrawal of no request for examination | ||
| WITN | Application deemed withdrawn, e.g. because no request for examination was filed or no examination fee was paid |